Structural and functional insights into tRNA binding and adenosine N1-methylation by an archaeal Trm10 homologue

DOI: 10.1093/nar/gkv1369
PMID: 26673726

Authors: Bart Van Laer (Vrije Universiteit Brussel) , Martine Roovers (Institut de Recherches Microbiologiques Jean-Marie Wiame) , Lina Wauters (Vrije Universiteit Brussel) , Joanna M. Kasprzak (International Institute of Molecular and Cell Biology in Warsaw) , Michal Dyzma (International Institute of Molecular and Cell Biology in Warsaw) , Egon Deyaert (Vrije Universiteit Brussel) , Ranjan Kumar singh (Vrije Universiteit Brussel) , André Feller (Université libre de Bruxelles) , Janusz M. Bujnicki (International Institute of Molecular and Cell Biology in Warsaw) , Louis Droogmans (Université libre de Bruxelles) , Wim Versees (Vrije Universiteit Brussel)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nucleic Acids Research

State: Published (Approved)
Published: December 2015
Diamond Proposal Number(s): 9426

Abstract: Purine nucleosides on position 9 of eukaryal and archaeal tRNAs are frequently modified in vivo by the post-transcriptional addition of a methyl group on their N1 atom. The methyltransferase Trm10 is responsible for this modification in both these domains of life. While certain Trm10 orthologues specifically methylate either guanosine or adenosine at position 9 of tRNA, others have a dual specificity. Until now structural information about this enzyme family was only available for the catalytic SPOUT domain of Trm10 proteins that show specificity toward guanosine. Here, we present the first crystal structure of a full length Trm10 orthologue specific for adenosine, revealing next to the catalytic SPOUT domain also N- and C-terminal domains. This structure hence provides crucial insights in the tRNA binding mechanism of this unique monomeric family of SPOUT methyltransferases. Moreover, structural comparison of this adenosine-specific Trm10 orthologue with guanosine-specific Trm10 orthologues suggests that the N1 methylation of adenosine relies on additional catalytic residues.

Diamond Keywords: Enzymes

Subject Areas: Biology and Bio-materials


Instruments: I24-Microfocus Macromolecular Crystallography

Other Facilities: Proxima 1 at Soleil

Added On: 18/01/2016 11:22

Documents:
gkv1369.pdf

Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)